Glycosidase activity in the excretory-secretory products of the liver fluke, Fasciola hepatica.

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Show simple item record Irwin, JA Morrissey, PE Ryan, JP Walshe, A O'Neill, SM Carrington, SD Matthews, E Fitzpatrick, E Mulcahy, G Corfield, AP Dalton, JP 2010-05-28T09:45:45Z 2004-10
dc.identifier.citation Parasitology, 2004, 129 (Pt 4), pp. 465 - 472
dc.identifier.issn 0031-1820
dc.identifier.other C1UNSUBMIT en_US
dc.description.abstract Fasciola hepatica secretes proteolytic enzymes and other molecules that are essential for host penetration and migration. This mixture may include enzymes required for the degradation of supramucosal gels, which defend epithelial surfaces against pathogen entry. These contain hydrated mucins that are heavily glycosylated. Excretory-secretory products (ES) from F. hepatica were examined for a range of glycosidase activities, using synthetic 4-methylumbelliferyl glycosides as substrates. The ES product contained at least 8 different glycosidase activities, the most abundant of which were beta-N-acetylhexosaminidase, beta-galactosidase and beta-glucosidase. Alpha-fucosidase, beta-glucuronidase, alpha-galactosidase, alpha-mannosidase and neuraminidase were also present. Beta-N-acetylhexosaminidase and beta-galactosidase were present in multiple isoforms (at least 4), whereas beta-glucosidase appeared to exist as one isoenzyme with a pI < 3.8. All three enzymes had acidic pH optima (4.5-5.0). Ovine small intestinal mucin was degraded by ES at pH 4.5 or 7.0, with or without active cathepsin L, the major protease found in F. hepatica ES. The ability of F. hepatica ES to degrade mucin in the presence or absence of active cathepsin L suggests that cathepsin L is not essential for mucin degradation. The abundance of beta-galactosidase and beta-hexosaminidase in ES supports a role for these enzymes in mucin degradation.
dc.format Print
dc.language eng
dc.relation.isbasedon 10.1017/s0031182004005803
dc.title Glycosidase activity in the excretory-secretory products of the liver fluke, Fasciola hepatica.
dc.type Journal Article
dc.parent Parasitology
dc.journal.volume Pt 4
dc.journal.volume 129
dc.journal.number en_US
dc.publocation New York, USA en_US
dc.identifier.startpage 465 en_US
dc.identifier.endpage 472 en_US SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 0601 Biochemistry and Cell Biology
dc.personcode 030896
dc.percentage 100 en_US Biochemistry and Cell Biology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US en_US
dc.location.activity en_US
dc.description.keywords Animals
dc.description.keywords Cattle
dc.description.keywords Fascioliasis
dc.description.keywords Hymecromone
dc.description.keywords Glycoside Hydrolases
dc.description.keywords beta-Galactosidase
dc.description.keywords beta-Glucosidase
dc.description.keywords Isoenzymes
dc.description.keywords Glycosides
dc.description.keywords Mucins
dc.description.keywords Helminth Proteins
dc.description.keywords Chromatography, Agarose
dc.description.keywords Histocytochemistry
dc.description.keywords beta-N-Acetylhexosaminidases
dc.description.keywords Cattle Diseases
dc.description.keywords Molecular Weight
dc.description.keywords Fasciola hepatica
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
utslib.copyright.status Open Access 2015-04-15 12:23:47.074767+10
pubs.consider-herdc false
utslib.collection.history General (ID: 2)

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